1xic
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(New page: 200px<br /><applet load="1xic" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xic, resolution 1.6Å" /> '''MODES OF BINDING SUBS...)
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Revision as of 03:58, 21 November 2007
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MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE
Overview
Studies of binding of substrates and inhibitors of the enzyme D-xylose, isomerase show, from X-ray diffraction data at 1.6-1.9 A resolution, that, there are a variety of binding modes. These vary in the manner in which, the substrate or its analogue extend, on binding, across the carboxy end, of the (betaalpha)(8)-barrel structure. These binding sites are His54 and, the metal ion (magnesium or manganese) that is held in place by Glul81, Asp245, Glu217 and Asp287. Possible catalytic groups have been identified, in proposed mechanisms and their role in the binding of ligands is, illustrated.
About this Structure
1XIC is a Single protein structure of sequence from Streptomyces rubiginosus with XLS and MN as ligands. Active as Xylose isomerase, with EC number 5.3.1.5 Full crystallographic information is available from OCA.
Reference
Modes of binding substrates and their analogues to the enzyme D-xylose isomerase., Carrell HL, Hoier H, Glusker JP, Acta Crystallogr D Biol Crystallogr. 1994 Mar 1;50(Pt 2):113-23. PMID:15299449
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